a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and regulates its activity, near-irreversible binding, modeling, overview

isoforms trypsin IV and trypsin I can stimulate epithelial sodium channel heterologously expressed in Xenopus oocytes. Epithelial sodium channel cleavage and activation by trypsin IV but not by trypsin I requires a critical cleavage site, i.e. Lys189 in the extracellular domain of the gamma-subunit. Channel activation by trypsin I is prevented by mutating three putative cleavage sites (Lys168, Lys170, and Arg172) in addition to mutating previously described prostasin (RKRK178), plasmin (Lys189), and neutrophil elastase (Val182 and Val193) sites

i.e. BvvTI, a Kunitz-type inhibitor from seeds of the Camel’s foot tree, Bauhinia variegata var. variegata. The inhibitor is also capable of significant inhibition of the proliferation of nasopharyngeal cancer CNE-1 cells in a selective way and of inhibiting anti-HIV-1 reverse transcriptase activity, overview

CnSPI, several inhibitor variants, separation by trypsin affinity chromatography. Possible regulatory role for CnSPIs in the endogenous proteolytic system of Clitocybe nebularis. Isolation from frozen fruiting bodies or basidiocarps

HV-BBI is a Bowman-Birk type protease inhibitor from the skin secretion of the Chinese Bamboo odorous frog Huia versabilis, SVIGCWTKSIPPRPCFVK-amide is a synthetic replicate of HV-BBI with the wild-type K (Lys8) residue in the presumed P1 position and is a potent, competitive, and reversible inhibitor of trypsin

HV-BBI is a Bowman-Birk type protease inhibitor from the skin secretion of the Chinese Bamboo odorous frog Huia versabilis, SVIGCWTRSIPPRPCFVK-amide is a synthetic replicate of HV-BBI with the mutant R (Arg8) residue in the presumed P1 position and is a competitive, and reversible inhibitor of trypsin with reduced potency compared to the wild type peptide SVIGCWTKSIPPRPCFVK-amide

identification of trypsin-3 binding peptides, and molecular modeling of the binding of peptides to isozyme trypsin-3. The degradation rate of peptides by trypsin correlates to their inhibitory efficacy, the most stable peptides being the most effective inhibitors, overview

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and protects it against autodigestion. Trypsin retains 40% of activity at constant level between 20 and 26 days in presence of the extract against complete inactivation in its absence. The peptide-trypsin complex is dissociated in presence of high concentration of substrates

[STUDIES ON THE EFFECTS OF A TRYPSIN INHIBITOR (TRASYLOL) ON ENZYME ACTIVITIES AND MORPHOLOGY IN TAUROCHOLATE AND CALCIPHYLAXIS PANCREATITIS OF THE RAT (A CONTRIBUTION TO THE PATHOGENESIS OF PANCREATITIS. II.)]

Behaviour of serum immunoreactive trypsin after serum activation by enterokinase in normal and cystic fibrosis patients. Evidence of a trypsin-alpha 1-proteinase inhibitor complex in some cystic fibrosis patients.

Levels and molecular forms of immunoreactive trypsin and chymotrypsin in amniotic fluids from normal and cystic fibrosis fetus: evidence for a lack of activation of proteolytic zymogens in cystic fibrosis fetus.